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Literature summary for 6.3.4.10 extracted from

  • Bao, B.; Wijeratne, S.S.; Rodriguez-Melendez, R.; Zempleni, J.
    Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity (2011), Biochem. Biophys. Res. Commun., 412, 115-120.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in HEK-293 cells Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm localizes predominantly in the cytoplasm Homo sapiens 5737
-
nucleus
-
Homo sapiens 5634
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
115000
-
N-terminal glutathione S transferase-tagged enzyme, x * 115000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] Homo sapiens
-
AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
Homo sapiens AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]
-
?

Subunits

Subunits Comment Organism
? N-terminal glutathione S transferase-tagged enzyme, x * 115000, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
HLCS
-
Homo sapiens
Holocarboxylase synthetase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
Homo sapiens